7AOS

crystal structure of the RARalpha/RXRalpha ligand binding domain heterodimer in complex with a fragment of SRC1 coactivator

7AOS の概要

• エントリーDOI: 10.2210/pdb7aos/pdb
• 分子名称: Retinoic acid receptor RXR-alpha, Retinoic acid receptor alpha, Nuclear receptor coactivator 1, ... (7 entities in total)
• 機能のキーワード: transcription factor, nuclear hormone receptor, coactivator, agonist, complex, hormone
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63565.48

構造登録者

le Maire, A.,Guee, L.,Bourguet, W. (登録日: 2020-10-15, 公開日: 2021-08-04, 最終更新日: 2024-01-31)

主引用文献

Senicourt, L.,le Maire, A.,Allemand, F.,Carvalho, J.E.,Guee, L.,Germain, P.,Schubert, M.,Bernado, P.,Bourguet, W.,Sibille, N.
Structural Insights into the Interaction of the Intrinsically Disordered Co-activator TIF2 with Retinoic Acid Receptor Heterodimer (RXR/RAR).
J.Mol.Biol., 433:166899-166899, 2021

PubMed Abstract: Retinoic acid receptors (RARs) and retinoid X receptors (RXRs) form heterodimers that activate target gene transcription by recruiting co-activator complexes in response to ligand binding. The nuclear receptor (NR) co-activator TIF2 mediates this recruitment by interacting with the ligand-binding domain (LBD) of NRs trough the nuclear receptor interaction domain (TIF2) containing three highly conserved α-helical LxxLL motifs (NR-boxes). The precise binding mode of this domain to RXR/RAR is not clear due to the disordered nature of TIF2. Here we present the structural characterization of TIF2 by integrating several experimental (NMR, SAXS, Far-UV CD, SEC-MALS) and computational data. Collectively, the data are in agreement with a largely disordered protein with partially structured regions, including the NR-boxes and their flanking regions, which are evolutionary conserved. NMR and X-ray crystallographic data on TIF2 in complex with RXR/RAR reveal a multisite binding of the three NR-boxes as well as an active role of their flanking regions in the interaction.

PubMed: 33647291
DOI: 10.1016/j.jmb.2021.166899

実験手法

X-RAY DIFFRACTION (2.55 Å)